Caging NLRP3 tames inflammasome activity

Kate Schroder; Rebecca C Coll

doi:10.1016/j.cell.2021.11.035

Caging NLRP3 tames inflammasome activity

Kate Schroder
, Rebecca C Coll

Research output: Contribution to journal › Article

11 Citations (Scopus)

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Abstract

How the danger sensor NLRP3 is activated is intensively debated. Using cryo-electron microscopy (EM) approaches, Andreeva and colleagues made the remarkable discovery that inactive NLRP3 forms a double ring of 12-16 monomers that shield its pyrin domains from the cytosol. We discuss this surprising new mechanism of inflammasome regulation.

Original language	English
Pages (from-to)	6224-6226
Number of pages	3
Journal	Cell
Volume	184
Issue number	26
DOIs	https://doi.org/10.1016/j.cell.2021.11.035
Publication status	Published - 22 Dec 2021

Bibliographical note

Keywords

Cryoelectron Microscopy
Cytosol
Inflammasomes
NLR Family, Pyrin Domain-Containing 3 Protein

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10.1016/j.cell.2021.11.035Licence: Unspecified

Caging NLRP3 tames inflammasome activity
Copyright 2021 Elsevier. This manuscript is distributed under a Creative Commons Attribution-NonCommercial-NoDerivs License (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits distribution and reproduction for non-commercial purposes, provided the author and source are cited.
Accepted author manuscript, 280 KBLicence: CC BY-NC-ND

Cite this

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abstract = "How the danger sensor NLRP3 is activated is intensively debated. Using cryo-electron microscopy (EM) approaches, Andreeva and colleagues made the remarkable discovery that inactive NLRP3 forms a double ring of 12-16 monomers that shield its pyrin domains from the cytosol. We discuss this surprising new mechanism of inflammasome regulation. ",

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AU - Coll, Rebecca C

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KW - Cryoelectron Microscopy

KW - Cytosol

KW - Inflammasomes

KW - NLR Family, Pyrin Domain-Containing 3 Protein

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Caging NLRP3 tames inflammasome activity

Abstract

Bibliographical note

Keywords

Access to Document

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Cite this